More recently, it has been reported that Pin1, a prolyl isomerase, interacts with FBXW7α in a phosphorylation-dependent manner and promotes FBXW7α auto-ubiquitination and protein degradation by disrupting FBXW7α dimerization, suggesting that inhibition of Pin1 could upregulate the expression of FBXW7α to retard the growth of human tumor cells [13]. This evidence concerns the gene PIN1 and neoplasm.